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Structure of the HRV-C 3C-Rupintrivir Complex Provides New Insights for Inhibitor Design.
Yuan, Shuai; Fan, Kaiyue; Chen, Zhonghao; Sun, Yao; Hou, Hai; Zhu, Ling.
Afiliación
  • Yuan S; CAS Key Laboratory of Infection and Immunity, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
  • Fan K; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
  • Chen Z; CAS Key Laboratory of Infection and Immunity, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
  • Sun Y; Beijing Forestry University, No. 35 Tsinghua East Road, Haidian District, Beijing, 100083, China.
  • Hou H; Key Laboratory for Space Bioscience and Space Biotechnology, School of Life Sciences, Northwestern Polytechnical University, Xi'an, 710072, China.
  • Zhu L; Institute of Medical Research, Northwestern Polytechnical University, Xi'an, 710072, China.
Virol Sin ; 35(4): 445-454, 2020 Aug.
Article en En | MEDLINE | ID: mdl-32103448
Human rhinoviruses (HRVs) are the predominant infectious agents for the common cold worldwide. The HRV-C species cause severe illnesses in children and are closely related to acute exacerbations of asthma. 3C protease, a highly conserved enzyme, cleaves the viral polyprotein during replication and assists the virus in escaping the host immune system. These key roles make 3C protease an important drug target. A few structures of 3Cs complexed with an irreversible inhibitor rupintrivir have been determined. These structures shed light on the determinants of drug specificity. Here we describe the structures of HRV-C15 3C in free and inhibitor-bound forms. The volume-decreased S1' subsite and half-closed S2 subsite, which were thought to be unique features of enterovirus A 3C proteases, appear in the HRV-C 3C protease. Rupintrivir assumes an "intermediate" conformation in the complex, which might open up additional avenues for the design of potent antiviral inhibitors. Analysis of the features of the three-dimensional structures and the amino acid sequences of 3C proteases suggest new applications for existing drugs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Antivirales / Fenilalanina / Pirrolidinonas / Valina / Diseño de Fármacos / Enterovirus Humano A / Proteasas Virales 3C / Isoxazoles Idioma: En Revista: Virol Sin Asunto de la revista: VIROLOGIA Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Antivirales / Fenilalanina / Pirrolidinonas / Valina / Diseño de Fármacos / Enterovirus Humano A / Proteasas Virales 3C / Isoxazoles Idioma: En Revista: Virol Sin Asunto de la revista: VIROLOGIA Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos